ID A0A1Y1VPW1_9FUNG Unreviewed; 1129 AA.
AC A0A1Y1VPW1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ORX61173.1};
GN ORFNames=BCR36DRAFT_439738 {ECO:0000313|EMBL:ORX61173.1};
OS Piromyces finnis.
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Neocallimastigomycetes; Neocallimastigales;
OC Neocallimastigaceae; Piromyces.
OX NCBI_TaxID=1754191 {ECO:0000313|EMBL:ORX61173.1, ECO:0000313|Proteomes:UP000193719};
RN [1] {ECO:0000313|EMBL:ORX61173.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Haitjema C.H., Gilmore S.P., Henske J.K., Solomon K.V., De Groot R.,
RA Kuo A., Mondo S.J., Salamov A.A., Labutti K., Zhao Z., Chiniquy J.,
RA Barry K., Brewer H.M., Purvine S.O., Wright A.T., Boxma B., Van Alen T.,
RA Hackstein J.H., Baker S.E., Grigoriev I.V., O'Malley M.A.;
RT "Genomes of anaerobic fungi encode conserved fungal cellulosomes for
RT biomass hydrolysis.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ORX61173.1, ECO:0000313|Proteomes:UP000193719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=finn {ECO:0000313|Proteomes:UP000193719};
RG DOE Joint Genome Institute;
RA Mondo S.J., Dannebaum R.O., Kuo R.C., Labutti K., Haridas S., Kuo A.,
RA Salamov A., Ahrendt S.R., Lipzen A., Sullivan W., Andreopoulos W.B.,
RA Clum A., Lindquist E., Daum C., Ramamoorthy G.K., Gryganskyi A., Culley D.,
RA Magnuson J.K., James T.Y., O'Malley M.A., Stajich J.E., Spatafora J.W.,
RA Visel A., Grigoriev I.V.;
RT "Pervasive Adenine N6-methylation of Active Genes in Fungi.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000256|ARBA:ARBA00004134}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|ARBA:ARBA00008314,
CC ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ORX61173.1}.
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DR EMBL; MCFH01000001; ORX61173.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1VPW1; -.
DR STRING; 1754191.A0A1Y1VPW1; -.
DR EnsemblFungi; ORX61173; ORX61173; BCR36DRAFT_439738.
DR OrthoDB; 1094820at2759; -.
DR Proteomes; UP000193719; Unassembled WGS sequence.
DR GO; GO:0030479; C:actin cortical patch; IEA:UniProtKB-SubCell.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003774; F:cytoskeletal motor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 1.10.10.820; -; 1.
DR Gene3D; 1.20.5.4820; -; 1.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR13140:SF729; HEAVY CHAIN, UNCONVENTIONAL MYOSIN; 1.
DR PANTHER; PTHR13140; MYOSIN; 1.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 3: Inferred from homology;
KW Actin-binding {ECO:0000256|ARBA:ARBA00023203, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00023212};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782};
KW Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW Reference proteome {ECO:0000313|Proteomes:UP000193719};
KW SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW ProRule:PRU00192}.
FT DOMAIN 35..708
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT DOMAIN 746..940
FT /note="TH1"
FT /evidence="ECO:0000259|PROSITE:PS51757"
FT DOMAIN 1070..1129
FT /note="SH3"
FT /evidence="ECO:0000259|PROSITE:PS50002"
FT REGION 585..607
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 924..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1039..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1039..1055
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1057..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 128..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
SQ SEQUENCE 1129 AA; 128310 MW; 68F7C7EFA6F6E652 CRC64;
MTQLINKLYK IYIFIFTNDI YLNKKIKILI IYNKKGVEDM VLLSKVTEEQ IVDNLRKRYQ
NDLIYTYIGP TLVAVNPYKQ LPYFTQKEID MYRGAASHEN APHIYATADT MFQNMMTDEE
NQCVIISGES GAGKTESAKL IIGGSGSNIV EQVKNIILGS NPLLESFGNA KTLRNNNSSR
FGKYFEIRFL RGGQPVGGNI SNFLLEKSRV VSPGKGERNF HIFYQLTKNV TEKDRTELGL
SAPSNFNYLN CSGTYDADGI DDTKEYAEMK KSLTICGVSE EDQNSLFQIV AGILHLGNID
FTEENNEAVV IDPRTLEFPA YLLGVSADAL HDKLVSRLMQ TGFMKKRQSD IRMTLNREQA
CSSRDALAKA LYSRMFDWLV QEINIAMKKL QGSNQDQILN LGVLDIYGFE IFEKNGFEQF
CINYVNERLQ QIFIELTLKS EQEEYVHENI QWVPIEFFNN KVVVDLIESK RPPGIMCILD
DVCATTHAVS KGSDEDFVRK MDSNCGDSKH YQGMQTKFLI RHYAGPVTYD CEGFCEANKD
TLFKDLIILM QTTTKPFIRN LFPENIDADD KKRPTTFSFK IKSQCHELVD TLMKCTPSYV
RCIKPNENKV PKEWDSKRVE HQTHYLNLKE NIKVRRAGFC YRQTFEKMLK RYAILTPETY
PSWNGNPKDG VKHILEAVDM DKDQWQFGLT KVFIKTPESL FILEELRDRK YHGYAKTIQT
CYRKWKSRKY FLDLKKEATD IFYNKKQRRR FSINRDFNGD YINYLSNPIL KQLVGKNEKV
YFASEMNKFD RKFKNVSIFD FIIGEQTVYF IGKEKAKKGP NKGKFIKVVK RAVPIDLITG
VSTSALADDI IVFHLPEYDY VCENVFKTEL VTILNNQYKK HTNRTLSITI NNTINYTVKK
TKWSGGGVYN LQFIEDPSIP TNIEGTTGIP KAGKAMTKPK NKGAEIRMPP GLPASTKPVH
KEPPVNTYHA PEKKYIQPAA ASSTPAATYT PAAAPVSATP SAQISNPISS SILAKAQSIN
TNLSSLANPP VAQQVKVTKA GTTPKSITSP VNPKISQIKK RPPPTPPPKK KLPTVKAIYA
YQASEADELS FNAGDIIYVI SKDESGWWTG VKQGEQKKGL FPSNYVQEN
//
